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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
2001-5-4
pubmed:abstractText
We analyzed the tissue distribution of apelin mRNA in rats by a quantitative reverse transcription-polymerase chain reaction and that of immunoreactive apelin (ir-apelin) by an enzyme immunoassay (EIA) using a monoclonal antibody. The expression levels of apelin mRNA and ir-apelin seemed to be consistent among tissues: they were highly expressed in the lung and mammary gland. By the combination of gel filtration and EIA, we found that the molecular forms of apelin differ among respective tissues: apelin molecules with sizes close to apelin-36 (long forms) were major components in the lung, testis, and uterus, but both long and short (whose sizes were close to [<Glu(65)]apelin-13) forms were detected in the mammary gland. In Scatchard analyses, the radioiodinated apelin-36 analogue bound to the receptor, APJ, with high affinity. In competitive binding assays, apelin-36 and apelin-19 far more efficiently inhibited the binding of the labeled apelin-36 analogue with APJ than [<Glu(65)]apelin-13. In analyses for the dissociation of apelin from APJ, unlabeled apelin-36 replaced more rapidly the labeled apelin-36 analogue bound with APJ than [<Glu(65)]apelin-13. Our results demonstrate that the long and short forms of apelin differently interact with APJ.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
1538
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
162-71
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:11336787-Amino Acid Sequence, pubmed-meshheading:11336787-Animals, pubmed-meshheading:11336787-Carrier Proteins, pubmed-meshheading:11336787-Chromatography, Gel, pubmed-meshheading:11336787-Female, pubmed-meshheading:11336787-Immunoenzyme Techniques, pubmed-meshheading:11336787-Intercellular Signaling Peptides and Proteins, pubmed-meshheading:11336787-Lung, pubmed-meshheading:11336787-Male, pubmed-meshheading:11336787-Mammary Glands, Animal, pubmed-meshheading:11336787-Molecular Sequence Data, pubmed-meshheading:11336787-Molecular Weight, pubmed-meshheading:11336787-RNA, Messenger, pubmed-meshheading:11336787-Rats, pubmed-meshheading:11336787-Rats, Wistar, pubmed-meshheading:11336787-Receptors, Dopamine D2, pubmed-meshheading:11336787-Receptors, G-Protein-Coupled, pubmed-meshheading:11336787-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:11336787-Testis, pubmed-meshheading:11336787-Uterus
pubmed:year
2001
pubmed:articleTitle
Molecular properties of apelin: tissue distribution and receptor binding.
pubmed:affiliation
Discovery Research Laboratories 1, Pharmaceutical Discovery Research Division, Takeda Chemical Industries, Ltd., Wadai 10, Tsukuba, 300-4293, Ibaraki, Japan.
pubmed:publicationType
Journal Article, Comparative Study